CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004579
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylyl cyclase-associated protein 
Protein Synonyms/Alias
 CAP 
Gene Name
 SRV2 
Gene Synonyms/Alias
 CAP1; YNL138W; N1210; N1838 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
15MQGYNLVKLLKRLEEacetylation[1]
49LEASKNNKPSDSGADubiquitination[2]
155IIKLGQLKESNRQSKubiquitination[2]
205FWTNRILKEYRESDPacetylation[1]
233DNLKAYIKEYHTTGVacetylation[1]
516KHSFADGKFKSAVFEacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control. 
Sequence Annotation
 DOMAIN 369 504 C-CAP/cofactor C-like.
 REGION 1 168 Adenyl cyclase-binding.
 REGION 354 361 Interaction with SH3 domain of ABP1.
 REGION 370 526 Dimerization and actin-binding.
 MOTIF 169 369 SH3-binding.
 MOD_RES 454 454 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 526 AA 
Protein Sequence
MPDSKYTMQG YNLVKLLKRL EEATARLEDV TIYQEGYIQN KLEASKNNKP SDSGADANTT 60
NEPSAENAPE VEQDPKCITA FQSYIGENID PLVELSGKID TVVLDALQLL KGGFQSQLTF 120
LRAAVRSRKP DYSSQTFADS LRPINENIIK LGQLKESNRQ SKYFAYLSAL SEGAPLFSWV 180
AVDTPVSMVT DFKDAAQFWT NRILKEYRES DPNAVEWVKK FLASFDNLKA YIKEYHTTGV 240
SWKKDGMDFA DAMAQSTKNT GATSSPSPAS ATAAPAPPPP PPAPPASVFE ISNDTPATSS 300
DANKGGIGAV FAELNQGENI TKGLKKVDKS QQTHKNPELR QSSTVSSTGS KSGPPPRPKK 360
PSTLKTKRPP RKELVGNKWF IENYENETES LVIDANKDES IFIGKCSQVL VQIKGKVNAI 420
SLSETESCSV VLDSSISGMD VIKSNKFGIQ VNHSLPQISI DKSDGGNIYL SKESLNTEIY 480
TSCSTAINVN LPIGEDDDYV EFPIPEQMKH SFADGKFKSA VFEHAG 526 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0008179; F:adenylate cyclase binding; TAS:SGD.
 GO:0008092; F:cytoskeletal protein binding; TAS:SGD.
 GO:0000902; P:cell morphogenesis; IEA:InterPro.
 GO:0007010; P:cytoskeleton organization; TAS:SGD.
 GO:0007265; P:Ras protein signal transduction; IMP:SGD. 
Interpro
 IPR001837; Adenylate_cyclase-assoc_CAP.
 IPR013912; Adenylate_cyclase-assoc_CAP_C.
 IPR013992; Adenylate_cyclase-assoc_CAP_N.
 IPR017901; C-CAP_CF_C-like.
 IPR016098; CAP/MinC_C.
 IPR018106; CAP_CS.
 IPR006599; CARP_motif. 
Pfam
 PF08603; CAP_C
 PF01213; CAP_N 
SMART
 SM00673; CARP 
PROSITE
 PS51329; C_CAP_COFACTOR_C
 PS01088; CAP_1
 PS01089; CAP_2 
PRINTS